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来自大肠杆菌的EcoR124I核酸内切酶HsdR亚基的纯化、结晶及初步X射线分析

Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli.

作者信息

Lapkouski Mikalai, Panjikar Santosh, Kuta Smatanova Ivana, Csefalvay Eva

机构信息

Institute of Physical Biology, University of South Bohemia in Ceske Budejovice, Zamek 136, CZ-373 33 Nove Hrady, Czech Republic.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt 7):582-5. doi: 10.1107/S174430910702622X. Epub 2007 Jun 11.

DOI:10.1107/S174430910702622X
PMID:17620716
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2335136/
Abstract

EcoR124I is a multicomplex enzyme belonging to the type I restriction-modification system from Escherichia coli. Although EcoR124I has been extensively characterized biochemically, there is no direct structural information available about particular subunits. HsdR is a motor subunit that is responsible for ATP hydrolysis, DNA translocation and cleavage of the DNA substrate recognized by the complex. Recombinant HsdR subunit was crystallized using the sitting-drop vapour-diffusion method. Crystals belong to the primitive monoclinic space group, with unit-cell parameters a = 85.75, b = 124.71, c = 128.37 A, beta = 108.14 degrees. Native data were collected to 2.6 A resolution at the X12 beamline of EMBL Hamburg.

摘要

EcoR124I是一种属于大肠杆菌I型限制修饰系统的多亚基复合酶。尽管EcoR124I已在生化方面得到广泛表征，但尚无关于特定亚基的直接结构信息。HsdR是一种驱动亚基，负责ATP水解、DNA转位以及复合物识别的DNA底物的切割。采用坐滴气相扩散法使重组HsdR亚基结晶。晶体属于原始单斜空间群，晶胞参数为a = 85.75、b = 124.71、c = 128.37 Å，β = 108.14°。在欧洲分子生物学实验室汉堡分部的X12光束线收集到分辨率为2.6 Å的天然数据。

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